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Structure-activity relationships of a novel capsid targeted inhibitor of HIV-1 replication
Journal article   Open access   Peer reviewed

Structure-activity relationships of a novel capsid targeted inhibitor of HIV-1 replication

Sandhya Kortagere, Jimmy P Xu, Marie K Mankowski, Roger G Ptak and Simon Cocklin
Journal of chemical information and modeling, v 54(11), pp 3080-3090
24 Nov 2014
PMID: 25302989
url
https://doi.org/10.1021/ci500437rView
Published, Version of Record (VoR) Open

Abstract

Anti-HIV Agents - pharmacology Virus Replication - drug effects Anti-HIV Agents - chemistry HIV-1 - physiology Capsid Proteins - antagonists & inhibitors HIV-1 - drug effects Humans Structure-Activity Relationship
Despite the considerable successes of highly active antiretroviral therapy (HAART) for the treatment of HIV/AIDS, cumulative drug toxicities and the development of multidrug-resistant virus necessitate the search for new classes of antiretroviral agents with novel modes of action. The HIV-1 capsid (CA) protein has been structurally and functionally characterized as a druggable target. We have recently designed a novel small molecule inhibitor I-XW-053 using the hybrid structure based method to block the interface between CA N-terminal domains (NTD-NTD interface) with micromolar affinity. In an effort to optimize and improve the efficacy of I-XW-053, we have developed the structure activity relationship of I-XW-053 compound series using ligand efficiency methods. Fifty-six analogues of I-XW-053 were designed that could be subclassified into four different core domains based on their ligand efficiency values computed as the ratio of binding efficiency (BEI) and surface efficiency (SEI) indices. Compound 34 belonging to subcore-3 showed an 11-fold improvement over I-XW-053 in blocking HIV-1 replication in primary human peripheral blood mononuclear cells (PBMCs). Surface plasmon resonance experiments confirmed the binding of compound 34 to purified HIV-1 CA protein. Molecular docking studies on compound 34 and I-XW-053 to HIV-1 CA protein suggested that they both bind to NTD-NTD interface region but with different binding modes, which was further validated using site-directed mutagenesis studies.

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Web of Science research areas
Chemistry, Medicinal
Chemistry, Multidisciplinary
Computer Science, Information Systems
Computer Science, Interdisciplinary Applications
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